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Conserved domains on  [gi|1958699163|ref|XP_038951343|]
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protein artemis isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
93-197 1.45e-25

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


:

Pssm-ID: 429512  Cd Length: 108  Bit Score: 101.20  E-value: 1.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699163  93 PDILHHLTTD-RNTQIHACRHPKAEeyfqWNKLPCGMASKTKTVLHTISIKPSTmwFGERTRKTNVIVRTGES------S 165
Cdd:pfam07522   1 PEILSLLTTDpLSTQIHVVPMPKLS----YEALLDYLTARKDHFDSVLAIRPTG--WTYRPPKTEVSDRIGPSirgritI 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958699163 166 YRACFSFHSSYSEIKDFLSYICPVNAYPNVIP 197
Cdd:pfam07522  75 YGVPYSEHSSFDELKEFVQFLRPKKIIPTVNV 106
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
1-25 1.08e-10

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


The actual alignment was detected with superfamily member cd16297:

Pssm-ID: 451500  Cd Length: 171  Bit Score: 60.60  E-value: 1.08e-10
                          10        20
                  ....*....|....*....|....*
gi 1958699163   1 MELLHSGGRVKDIQSVYLDTTFCDP 25
Cdd:cd16297   147 MELLHSGDRVKDIQSVYLDTTFCDP 171
 
Name Accession Description Interval E-value
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
93-197 1.45e-25

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


Pssm-ID: 429512  Cd Length: 108  Bit Score: 101.20  E-value: 1.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699163  93 PDILHHLTTD-RNTQIHACRHPKAEeyfqWNKLPCGMASKTKTVLHTISIKPSTmwFGERTRKTNVIVRTGES------S 165
Cdd:pfam07522   1 PEILSLLTTDpLSTQIHVVPMPKLS----YEALLDYLTARKDHFDSVLAIRPTG--WTYRPPKTEVSDRIGPSirgritI 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958699163 166 YRACFSFHSSYSEIKDFLSYICPVNAYPNVIP 197
Cdd:pfam07522  75 YGVPYSEHSSFDELKEFVQFLRPKKIIPTVNV 106
artemis-SNM1C-like_MBL-fold cd16297
artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease ...
1-25 1.08e-10

artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Inactivation of Artemis causes severe combined immunodeficiency (SCID). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293855  Cd Length: 171  Bit Score: 60.60  E-value: 1.08e-10
                          10        20
                  ....*....|....*....|....*
gi 1958699163   1 MELLHSGGRVKDIQSVYLDTTFCDP 25
Cdd:cd16297   147 MELLHSGDRVKDIQSVYLDTTFCDP 171
 
Name Accession Description Interval E-value
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
93-197 1.45e-25

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


Pssm-ID: 429512  Cd Length: 108  Bit Score: 101.20  E-value: 1.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699163  93 PDILHHLTTD-RNTQIHACRHPKAEeyfqWNKLPCGMASKTKTVLHTISIKPSTmwFGERTRKTNVIVRTGES------S 165
Cdd:pfam07522   1 PEILSLLTTDpLSTQIHVVPMPKLS----YEALLDYLTARKDHFDSVLAIRPTG--WTYRPPKTEVSDRIGPSirgritI 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958699163 166 YRACFSFHSSYSEIKDFLSYICPVNAYPNVIP 197
Cdd:pfam07522  75 YGVPYSEHSSFDELKEFVQFLRPKKIIPTVNV 106
artemis-SNM1C-like_MBL-fold cd16297
artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease ...
1-25 1.08e-10

artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Inactivation of Artemis causes severe combined immunodeficiency (SCID). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293855  Cd Length: 171  Bit Score: 60.60  E-value: 1.08e-10
                          10        20
                  ....*....|....*....|....*
gi 1958699163   1 MELLHSGGRVKDIQSVYLDTTFCDP 25
Cdd:cd16297   147 MELLHSGDRVKDIQSVYLDTTFCDP 171
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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